Characterization of an interesting selenium-dependent glutathione peroxidase (Se-GPx) protecting cells against environmental stress: The Camelus dromedarius erythrocytes Se-GPx

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dc.authorid57190409749
dc.authorid6507478596
dc.authorid56400331100
dc.authorid57201282307
dc.authorid7004132795
dc.contributor.authorChafik A.
dc.contributor.authorEssamadi A.
dc.contributor.authorÇelik S.Y.
dc.contributor.authorSolak K.
dc.contributor.authorMavi A.
dc.date.accessioned20.04.201910:49:12
dc.date.accessioned2019-04-20T21:42:58Z
dc.date.available20.04.201910:49:12
dc.date.available2019-04-20T21:42:58Z
dc.date.issued2019
dc.departmentBayburt Üniversitesien_US
dc.description.abstractCamel lives most of its life under high environmental stress in the desert. Glutathione peroxidase plays a key role in protecting cells against oxidative stress. For the first time, selenium-dependent glutathione peroxidase (Se-GPx) was purified from camel erythrocytes, biochemically characterized, and some of its properties were studied. The enzyme was purified using ethanol-chloroform treatment, acetone precipitation and ion exchange chromatography. A purification fold of 33.72 with 0.19% yield were obtained. The native molecular weight of the enzyme was estimated to be about 69 kDa. On SDS-PAGE, the enzyme was composed of two different subunits with a molecular weight of approximately 53 and 21 kDa. An optimum temperature of 47 °C and an optimum pH of 7.2 were found. The activation energy was 41.71 kJ/mol. This enzyme was inhibited by thiol reagents, D,L-Dithiothreitol and ?-Mercaptoethanol, and was sensitive to bivalent cations. The enzyme had a general specificity toward hydroperoxides, and high specificity for reduced glutathione. The purified enzyme contained 3.06 mol of selenium per mol of protein. The Km and Vmax values for hydrogen peroxide and reduced glutathione were 0.72 and 1.58 mM, and 25.33 and 31.03 U/mg, respectively. The biochemical properties of camel Se-GPx were different comparing to those of mammalian species. Lower molecular weight, heterodimeric structure, higher optimum temperature, relatively lower optimum pH, lower content of selenium and higher affinity for hydrogen peroxide at low reduced glutathione concentration, these could be explained by the fact that camel is able to live in the intense environmental stress in the desert. © 2019 Elsevier Ltden_US
dc.identifier.doi10.1016/j.bcab.2019.01.038
dc.identifier.issn1878-8181
dc.identifier.scopus2-s2.0-85060990480en_US
dc.identifier.scopusqualityQ1en_US
dc.identifier.urihttps://dx.doi.org/10.1016/j.bcab.2019.01.038
dc.identifier.urihttps://hdl.handle.net/20.500.12403/309
dc.identifier.volume18
dc.identifier.wosWOS:000469474200008en_US
dc.identifier.wosqualityN/Aen_US
dc.indekslendigikaynakWeb of Scienceen_US
dc.indekslendigikaynakScopusen_US
dc.language.isoenen_US
dc.publisherElsevier Ltd
dc.relation.ispartofBiocatalysis and Agricultural Biotechnologyen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectBiochemical properties
dc.subjectCamel
dc.subjectDesert
dc.subjectEnvironmental stress
dc.subjectGlutathione peroxidase
dc.subjectBiochemical properties
dc.subjectCamel
dc.subjectDesert
dc.subjectEnvironmental stress
dc.subjectGlutathione peroxidase
dc.titleCharacterization of an interesting selenium-dependent glutathione peroxidase (Se-GPx) protecting cells against environmental stress: The Camelus dromedarius erythrocytes Se-GPxen_US
dc.typeArticleen_US

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